New Quinoline Analogues: As Potential Diabetics Inhibitors and Molecular Docking Study

The 7-quinolinyl bearing 1,3,4-thiadiazole-2-amine analogues were synthesized (1–17) and based on the literature these analog were screened in vitro for their α-amylase and α-glucosidase inhibitory profile. All analogues showed moderate to good inhibitory potentials ranging between 0.80 ± 0.05 µM to 40.20 ± 0.70 µM and 1.20 ± 0.10 µM to 43.30 ± 0.80 µM against α-amylase and α-glucosidase. Among the series, analogues 2 (IC50 = 2.10 ± 0.10 µM), (IC50 = 2.40 ± 0.10 µM), 3 (IC50 = 0.80 ± 0.05 µM), (IC50 = 1.20 ± 0.10 µM) and 4 (IC50 = 1.50 ± 0.10 µM), (IC50 = 1.90 ± 0.10 µM) with flouro substitution at phenyl ring of the 1,3,4-thiadiazole ring were identified to be the most potent inhibitors against α-amylase and α-glucosidase enzymes. The structure of all the newly synthetics analogues were confirmed by using different types of spectroscopic techniques such as HREI-MS, 1H- and 13C-NMR spectroscopy. To find structure-activity relationship, molecular docking studies were carry out to understand the binding mode of active inhibitors with active site of enzymes and results supported the experimental data. Due to the most potent inhibitory activity of analogue 4 among all the synthesized compound, it was screened against streptozotocin induced diabetic animal model.</p

Evaluation of synthetic aminoquinoline derivatives as urease inhibitors: in vitro, in silico and kinetic studies

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Diphenyl-substituted triazine derivatives: synthesis, α-glucosidase inhibitory activity, kinetics and in silico studies

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Unsymmetrical thiourea derivatives: synthesis and evaluation as promising antioxidant and enzyme inhibitors

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Synthesis of indole derivatives as Alzheimer inhibitors and their molecular docking study

Acetylcholinesterase prevails in the healthy brain, with butyrylcholinesterase reflected to play a minor role in regulating brain acetylcholine (ACh) levels. However, BuChE activity gradually increases in patients with (AD), while AChE activity remains unaffected or decays. Both enzymes therefore represent legitimate therapeutic targets for ameliorating the cholinergic deficit considered to be responsible for the declines in cognitive, behavioural, and global functioning characteristic of AD. Current study described the synthesis of indole-based sulfonamide derivatives (1-23) and their biological activity. Synthesis of these scaffolds were achieved by mixing chloro-substituted indole bearing amine group with various substituted benzene sulfonyl chloride in pyridine, under refluxed condition to obtained desired products. All products were then evaluated for AchE and BuchE inhibitory potential compare with positive Donepezil as standard drug for both AchE and BchE having IC50 = 0.016 ± 0.12 and 0.30 ± 0.010 μM respectively. In this regard analog 9 was found potent having IC50 value 0.15 ± 0.050 μM and 0.20 ± 0.10 for both AchE and BuChE respectively. All other derivatives also found with better potential. All compounds were characterized by various techniques such as 1H, 13C-NMR and HREI-MS. In addition, biological activity was maintained to explore the bioactive nature of scaffolds and their protein-ligand interaction (PLI) was checked through molecular docking study. Communicated by Ramaswamy H. Sarma</p

Molecular Modeling and Synthesis of Indoline-2,3-dione-Based Benzene Sulfonamide Derivatives and Their Inhibitory Activity against α‑Glucosidase and α‑Amylase Enzymes

Diabetes is also known as a critical and noisy disease. Hyperglycemia, that is, increased blood glucose level is a common effect of uncontrolled diabetes, and over a period of time can cause serious effects on health such as blood vessel damage and nervous system damage. However, many attempts have been made to find suitable and beneficial solutions to overcome diabetes. Considering this fact, we synthesized a novel series of indoline-2,3-dione-based benzene sulfonamide derivatives and evaluated them against α-glucosidase and α-amylase enzymes. Out of the synthesized sixteen compounds (1–16), only three compounds showed better results; the IC50 value was in the range of 12.70 ± 0.20 to 0.90 ± 0.10 μM for α-glucosidase against acarbose 11.50 ± 0.30 μM and 14.90 ± 0.20 to 1.10 ± 0.10 μM for α-amylase against acarbose 12.20 ± 0.30 μM. Among the series, only three compounds showed better inhibitory potential such as analogues 11 (0.90 ± 0.10 μM for α-glucosidase and 1.10 ± 0.10 μM for α-amylase), 1 (1.10 ± 0.10 μM for α-glucosidase and 1.30 ± 0.10 μM for α-amylase), and 6 (1.20 ± 0.10 μM for α-glucosidase and 1.60 ± 0.10 μM for α-amylase). Molecular modeling was performed to determine the binding affinity of active interacting residues against these enzymes, and it was found that benzenesulfonohydrazide derivatives can be indexed as suitable inhibitors for diabetes mellitus